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8OZ0

Structure of a human 48S translation initiation complex with eIF4F and eIF4A

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
10000166molecular_functionnucleotide binding
10000339molecular_functionRNA cap binding
10002183biological_processcytoplasmic translational initiation
10003676molecular_functionnucleic acid binding
10003723molecular_functionRNA binding
10003724molecular_functionRNA helicase activity
10003725molecular_functiondouble-stranded RNA binding
10003729molecular_functionmRNA binding
10003743molecular_functiontranslation initiation factor activity
10004386molecular_functionhelicase activity
10005515molecular_functionprotein binding
10005524molecular_functionATP binding
10005634cellular_componentnucleus
10005737cellular_componentcytoplasm
10005829cellular_componentcytosol
10005886cellular_componentplasma membrane
10006412biological_processtranslation
10006413biological_processtranslational initiation
10008135molecular_functiontranslation factor activity, RNA binding
10010494cellular_componentcytoplasmic stress granule
10016020cellular_componentmembrane
10016281cellular_componenteukaryotic translation initiation factor 4F complex
10016787molecular_functionhydrolase activity
10016887molecular_functionATP hydrolysis activity
10045944biological_processpositive regulation of transcription by RNA polymerase II
10048471cellular_componentperinuclear region of cytoplasm
10070062cellular_componentextracellular exosome
10097165cellular_componentnuclear stress granule
20003723molecular_functionRNA binding
30000166molecular_functionnucleotide binding
30000339molecular_functionRNA cap binding
30002183biological_processcytoplasmic translational initiation
30003676molecular_functionnucleic acid binding
30003723molecular_functionRNA binding
30003724molecular_functionRNA helicase activity
30003725molecular_functiondouble-stranded RNA binding
30003729molecular_functionmRNA binding
30003743molecular_functiontranslation initiation factor activity
30004386molecular_functionhelicase activity
30005515molecular_functionprotein binding
30005524molecular_functionATP binding
30005634cellular_componentnucleus
30005737cellular_componentcytoplasm
30005829cellular_componentcytosol
30005886cellular_componentplasma membrane
30006412biological_processtranslation
30006413biological_processtranslational initiation
30008135molecular_functiontranslation factor activity, RNA binding
30010494cellular_componentcytoplasmic stress granule
30016020cellular_componentmembrane
30016281cellular_componenteukaryotic translation initiation factor 4F complex
30016787molecular_functionhydrolase activity
30016887molecular_functionATP hydrolysis activity
30045944biological_processpositive regulation of transcription by RNA polymerase II
30048471cellular_componentperinuclear region of cytoplasm
30070062cellular_componentextracellular exosome
30097165cellular_componentnuclear stress granule
50000184biological_processnuclear-transcribed mRNA catabolic process, nonsense-mediated decay
50000785cellular_componentchromatin
50001732biological_processformation of cytoplasmic translation initiation complex
50002183biological_processcytoplasmic translational initiation
50003723molecular_functionRNA binding
50003743molecular_functiontranslation initiation factor activity
50005515molecular_functionprotein binding
50005634cellular_componentnucleus
50005654cellular_componentnucleoplasm
50005737cellular_componentcytoplasm
50005829cellular_componentcytosol
50005852cellular_componenteukaryotic translation initiation factor 3 complex
50006412biological_processtranslation
50006413biological_processtranslational initiation
50006446biological_processregulation of translational initiation
50014069cellular_componentpostsynaptic density
50016020cellular_componentmembrane
50016282cellular_componenteukaryotic 43S preinitiation complex
50016605cellular_componentPML body
50032991cellular_componentprotein-containing complex
50033290cellular_componenteukaryotic 48S preinitiation complex
50045296molecular_functioncadherin binding
50045727biological_processpositive regulation of translation
50045947biological_processnegative regulation of translational initiation
50070062cellular_componentextracellular exosome
50071540cellular_componenteukaryotic translation initiation factor 3 complex, eIF3e
60001732biological_processformation of cytoplasmic translation initiation complex
60002183biological_processcytoplasmic translational initiation
60003743molecular_functiontranslation initiation factor activity
60004843molecular_functioncysteine-type deubiquitinase activity
60005515molecular_functionprotein binding
60005737cellular_componentcytoplasm
60005829cellular_componentcytosol
60005852cellular_componenteukaryotic translation initiation factor 3 complex
60006412biological_processtranslation
60006413biological_processtranslational initiation
60006508biological_processproteolysis
60008233molecular_functionpeptidase activity
60008234molecular_functioncysteine-type peptidase activity
60008237molecular_functionmetallopeptidase activity
60016020cellular_componentmembrane
60016282cellular_componenteukaryotic 43S preinitiation complex
60016787molecular_functionhydrolase activity
60031369molecular_functiontranslation initiation factor binding
60033290cellular_componenteukaryotic 48S preinitiation complex
60042802molecular_functionidentical protein binding
60045202cellular_componentsynapse
60071541cellular_componenteukaryotic translation initiation factor 3 complex, eIF3m
60075522biological_processIRES-dependent viral translational initiation
60101005molecular_functiondeubiquitinase activity
60140492molecular_functionmetal-dependent deubiquitinase activity
70001732biological_processformation of cytoplasmic translation initiation complex
70002183biological_processcytoplasmic translational initiation
70003676molecular_functionnucleic acid binding
70003723molecular_functionRNA binding
70003743molecular_functiontranslation initiation factor activity
70005515molecular_functionprotein binding
70005634cellular_componentnucleus
70005737cellular_componentcytoplasm
70005829cellular_componentcytosol
70005852cellular_componenteukaryotic translation initiation factor 3 complex
70006412biological_processtranslation
70006413biological_processtranslational initiation
70016282cellular_componenteukaryotic 43S preinitiation complex
70033290cellular_componenteukaryotic 48S preinitiation complex
70048471cellular_componentperinuclear region of cytoplasm
70075525biological_processviral translational termination-reinitiation
80001732biological_processformation of cytoplasmic translation initiation complex
80002183biological_processcytoplasmic translational initiation
80003723molecular_functionRNA binding
80003743molecular_functiontranslation initiation factor activity
80005515molecular_functionprotein binding
80005737cellular_componentcytoplasm
80005829cellular_componentcytosol
80005852cellular_componenteukaryotic translation initiation factor 3 complex
80006412biological_processtranslation
80006413biological_processtranslational initiation
80006446biological_processregulation of translational initiation
80008233molecular_functionpeptidase activity
80008237molecular_functionmetallopeptidase activity
80016020cellular_componentmembrane
80016282cellular_componenteukaryotic 43S preinitiation complex
80032435biological_processnegative regulation of proteasomal ubiquitin-dependent protein catabolic process
80033290cellular_componenteukaryotic 48S preinitiation complex
80070062cellular_componentextracellular exosome
80071541cellular_componenteukaryotic translation initiation factor 3 complex, eIF3m
80140492molecular_functionmetal-dependent deubiquitinase activity
90002181biological_processcytoplasmic translation
90003723molecular_functionRNA binding
90003730molecular_functionmRNA 3'-UTR binding
90003735molecular_functionstructural constituent of ribosome
90005515molecular_functionprotein binding
90005737cellular_componentcytoplasm
90005783cellular_componentendoplasmic reticulum
90005829cellular_componentcytosol
90005840cellular_componentribosome
90006412biological_processtranslation
90022625cellular_componentcytosolic large ribosomal subunit
90048027molecular_functionmRNA 5'-UTR binding
91990904cellular_componentribonucleoprotein complex
A0001732biological_processformation of cytoplasmic translation initiation complex
A0002183biological_processcytoplasmic translational initiation
A0002188biological_processtranslation reinitiation
A0003723molecular_functionRNA binding
A0003729molecular_functionmRNA binding
A0003743molecular_functiontranslation initiation factor activity
A0005198molecular_functionstructural molecule activity
A0005515molecular_functionprotein binding
A0005654cellular_componentnucleoplasm
A0005730cellular_componentnucleolus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005852cellular_componenteukaryotic translation initiation factor 3 complex
A0005874cellular_componentmicrotubule
A0006412biological_processtranslation
A0006413biological_processtranslational initiation
A0014069cellular_componentpostsynaptic density
A0016020cellular_componentmembrane
A0016282cellular_componenteukaryotic 43S preinitiation complex
A0030971molecular_functionreceptor tyrosine kinase binding
A0032991cellular_componentprotein-containing complex
A0033290cellular_componenteukaryotic 48S preinitiation complex
A0043226cellular_componentorganelle
A0043614cellular_componentmulti-eIF complex
A0070373biological_processnegative regulation of ERK1 and ERK2 cascade
A0071540cellular_componenteukaryotic translation initiation factor 3 complex, eIF3e
A0071541cellular_componenteukaryotic translation initiation factor 3 complex, eIF3m
A0075522biological_processIRES-dependent viral translational initiation
A0075525biological_processviral translational termination-reinitiation
B0001732biological_processformation of cytoplasmic translation initiation complex
B0002183biological_processcytoplasmic translational initiation
B0003723molecular_functionRNA binding
B0003743molecular_functiontranslation initiation factor activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005852cellular_componenteukaryotic translation initiation factor 3 complex
B0006412biological_processtranslation
B0006413biological_processtranslational initiation
B0006446biological_processregulation of translational initiation
B0016020cellular_componentmembrane
B0016282cellular_componenteukaryotic 43S preinitiation complex
B0033290cellular_componenteukaryotic 48S preinitiation complex
B0043022molecular_functionribosome binding
C0001732biological_processformation of cytoplasmic translation initiation complex
C0002183biological_processcytoplasmic translational initiation
C0003743molecular_functiontranslation initiation factor activity
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005852cellular_componenteukaryotic translation initiation factor 3 complex
C0006412biological_processtranslation
C0006413biological_processtranslational initiation
C0016282cellular_componenteukaryotic 43S preinitiation complex
C0031369molecular_functiontranslation initiation factor binding
C0032991cellular_componentprotein-containing complex
C0033290cellular_componenteukaryotic 48S preinitiation complex
C0071541cellular_componenteukaryotic translation initiation factor 3 complex, eIF3m
D0000423biological_processmitophagy
D0003676molecular_functionnucleic acid binding
D0003723molecular_functionRNA binding
D0003743molecular_functiontranslation initiation factor activity
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005739cellular_componentmitochondrion
D0005829cellular_componentcytosol
D0005850cellular_componenteukaryotic translation initiation factor 2 complex
D0006412biological_processtranslation
D0006413biological_processtranslational initiation
D0006417biological_processregulation of translation
D0010494cellular_componentcytoplasmic stress granule
D0016020cellular_componentmembrane
D0032057biological_processnegative regulation of translational initiation in response to stress
D0033290cellular_componenteukaryotic 48S preinitiation complex
D0034063biological_processstress granule assembly
D0034198biological_processcellular response to amino acid starvation
D0034599biological_processcellular response to oxidative stress
D0034605biological_processcellular response to heat
D0034644biological_processcellular response to UV
D0034976biological_processresponse to endoplasmic reticulum stress
D0036490biological_processregulation of translation in response to endoplasmic reticulum stress
D0036499biological_processPERK-mediated unfolded protein response
D0043022molecular_functionribosome binding
D0043558biological_processregulation of translational initiation in response to stress
D0044207cellular_componenttranslation initiation ternary complex
D0045202cellular_componentsynapse
D0070062cellular_componentextracellular exosome
D0097250biological_processmitochondrial respirasome assembly
D0097451cellular_componentglial limiting end-foot
D0140468biological_processHRI-mediated signaling
D1904373biological_processresponse to kainic acid
D1990737biological_processresponse to manganese-induced endoplasmic reticulum stress
D2000676biological_processpositive regulation of type B pancreatic cell apoptotic process
E0000049molecular_functiontRNA binding
E0000166molecular_functionnucleotide binding
E0001731biological_processformation of translation preinitiation complex
E0002183biological_processcytoplasmic translational initiation
E0003743molecular_functiontranslation initiation factor activity
E0003924molecular_functionGTPase activity
E0005515molecular_functionprotein binding
E0005525molecular_functionGTP binding
E0005634cellular_componentnucleus
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0005850cellular_componenteukaryotic translation initiation factor 2 complex
E0006412biological_processtranslation
E0006413biological_processtranslational initiation
E0008135molecular_functiontranslation factor activity, RNA binding
E0016787molecular_functionhydrolase activity
E0045296molecular_functioncadherin binding
E0070062cellular_componentextracellular exosome
E1990856molecular_functionmethionyl-initiator methionine tRNA binding
F0001732biological_processformation of cytoplasmic translation initiation complex
F0002183biological_processcytoplasmic translational initiation
F0003723molecular_functionRNA binding
F0003743molecular_functiontranslation initiation factor activity
F0005515molecular_functionprotein binding
F0005737cellular_componentcytoplasm
F0005829cellular_componentcytosol
F0005852cellular_componenteukaryotic translation initiation factor 3 complex
F0006412biological_processtranslation
F0006413biological_processtranslational initiation
F0016282cellular_componenteukaryotic 43S preinitiation complex
F0033290cellular_componenteukaryotic 48S preinitiation complex
F0045202cellular_componentsynapse
F0070062cellular_componentextracellular exosome
F0071541cellular_componenteukaryotic translation initiation factor 3 complex, eIF3m
G0000049molecular_functiontRNA binding
G0003723molecular_functionRNA binding
G0003743molecular_functiontranslation initiation factor activity
G0005515molecular_functionprotein binding
G0005737cellular_componentcytoplasm
G0005829cellular_componentcytosol
G0006412biological_processtranslation
G0006413biological_processtranslational initiation
G0008135molecular_functiontranslation factor activity, RNA binding
G0016282cellular_componenteukaryotic 43S preinitiation complex
G0033290cellular_componenteukaryotic 48S preinitiation complex
G0042255biological_processribosome assembly
G0043614cellular_componentmulti-eIF complex
G0045202cellular_componentsynapse
H0000166molecular_functionnucleotide binding
H0001732biological_processformation of cytoplasmic translation initiation complex
H0003723molecular_functionRNA binding
H0003743molecular_functiontranslation initiation factor activity
H0005092molecular_functionGDP-dissociation inhibitor activity
H0005096molecular_functionGTPase activator activity
H0005515molecular_functionprotein binding
H0005525molecular_functionGTP binding
H0005634cellular_componentnucleus
H0005737cellular_componentcytoplasm
H0005829cellular_componentcytosol
H0005886cellular_componentplasma membrane
H0006412biological_processtranslation
H0006413biological_processtranslational initiation
H0006446biological_processregulation of translational initiation
H0042255biological_processribosome assembly
H0045202cellular_componentsynapse
H0045296molecular_functioncadherin binding
H0071074molecular_functioneukaryotic initiation factor eIF2 binding
I0001732biological_processformation of cytoplasmic translation initiation complex
I0002183biological_processcytoplasmic translational initiation
I0003676molecular_functionnucleic acid binding
I0003723molecular_functionRNA binding
I0003743molecular_functiontranslation initiation factor activity
I0005515molecular_functionprotein binding
I0005737cellular_componentcytoplasm
I0005829cellular_componentcytosol
I0005852cellular_componenteukaryotic translation initiation factor 3 complex
I0006412biological_processtranslation
I0006413biological_processtranslational initiation
I0006446biological_processregulation of translational initiation
I0010494cellular_componentcytoplasmic stress granule
I0016282cellular_componenteukaryotic 43S preinitiation complex
I0031369molecular_functiontranslation initiation factor binding
I0033290cellular_componenteukaryotic 48S preinitiation complex
I0045202cellular_componentsynapse
I0060090molecular_functionmolecular adaptor activity
I0070062cellular_componentextracellular exosome
I0071541cellular_componenteukaryotic translation initiation factor 3 complex, eIF3m
I0075522biological_processIRES-dependent viral translational initiation
I0075525biological_processviral translational termination-reinitiation
J0001732biological_processformation of cytoplasmic translation initiation complex
J0002183biological_processcytoplasmic translational initiation
J0003723molecular_functionRNA binding
J0003743molecular_functiontranslation initiation factor activity
J0005515molecular_functionprotein binding
J0005737cellular_componentcytoplasm
J0005829cellular_componentcytosol
J0005852cellular_componenteukaryotic translation initiation factor 3 complex
J0006412biological_processtranslation
J0006413biological_processtranslational initiation
J0016282cellular_componenteukaryotic 43S preinitiation complex
J0031369molecular_functiontranslation initiation factor binding
J0033290cellular_componenteukaryotic 48S preinitiation complex
J0043022molecular_functionribosome binding
J0045727biological_processpositive regulation of translation
K0001650cellular_componentfibrillar center
K0001732biological_processformation of cytoplasmic translation initiation complex
K0002183biological_processcytoplasmic translational initiation
K0003723molecular_functionRNA binding
K0003743molecular_functiontranslation initiation factor activity
K0005515molecular_functionprotein binding
K0005654cellular_componentnucleoplasm
K0005730cellular_componentnucleolus
K0005737cellular_componentcytoplasm
K0005829cellular_componentcytosol
K0005852cellular_componenteukaryotic translation initiation factor 3 complex
K0006412biological_processtranslation
K0006413biological_processtranslational initiation
K0016020cellular_componentmembrane
K0016282cellular_componenteukaryotic 43S preinitiation complex
K0032991cellular_componentprotein-containing complex
K0033290cellular_componenteukaryotic 48S preinitiation complex
K0045202cellular_componentsynapse
K0075525biological_processviral translational termination-reinitiation
L0001843biological_processneural tube closure
L0002181biological_processcytoplasmic translation
L0003723molecular_functionRNA binding
L0003730molecular_functionmRNA 3'-UTR binding
L0003735molecular_functionstructural constituent of ribosome
L0005515molecular_functionprotein binding
L0005634cellular_componentnucleus
L0005654cellular_componentnucleoplasm
L0005730cellular_componentnucleolus
L0005737cellular_componentcytoplasm
L0005783cellular_componentendoplasmic reticulum
L0005813cellular_componentcentrosome
L0005829cellular_componentcytosol
L0005840cellular_componentribosome
L0005856cellular_componentcytoskeleton
L0005925cellular_componentfocal adhesion
L0006364biological_processrRNA processing
L0006412biological_processtranslation
L0010628biological_processpositive regulation of gene expression
L0014033biological_processneural crest cell differentiation
L0016020cellular_componentmembrane
L0019901molecular_functionprotein kinase binding
L0022626cellular_componentcytosolic ribosome
L0022627cellular_componentcytosolic small ribosomal subunit
L0032040cellular_componentsmall-subunit processome
L0032991cellular_componentprotein-containing complex
L0042274biological_processribosomal small subunit biogenesis
L0045202cellular_componentsynapse
L0048027molecular_functionmRNA 5'-UTR binding
L0050821biological_processprotein stabilization
L1902255biological_processpositive regulation of intrinsic apoptotic signaling pathway by p53 class mediator
L1904667biological_processnegative regulation of ubiquitin protein ligase activity
L1990904cellular_componentribonucleoprotein complex
L1990948molecular_functionubiquitin ligase inhibitor activity
L2000059biological_processnegative regulation of ubiquitin-dependent protein catabolic process
M0000028biological_processribosomal small subunit assembly
M0002181biological_processcytoplasmic translation
M0003677molecular_functionDNA binding
M0003723molecular_functionRNA binding
M0003735molecular_functionstructural constituent of ribosome
M0005515molecular_functionprotein binding
M0005634cellular_componentnucleus
M0005654cellular_componentnucleoplasm
M0005730cellular_componentnucleolus
M0005737cellular_componentcytoplasm
M0005829cellular_componentcytosol
M0005840cellular_componentribosome
M0006364biological_processrRNA processing
M0006412biological_processtranslation
M0008270molecular_functionzinc ion binding
M0014069cellular_componentpostsynaptic density
M0022626cellular_componentcytosolic ribosome
M0022627cellular_componentcytosolic small ribosomal subunit
M0032040cellular_componentsmall-subunit processome
M0042274biological_processribosomal small subunit biogenesis
M0046872molecular_functionmetal ion binding
M0098793cellular_componentpresynapse
M0098978cellular_componentglutamatergic synapse
M0098982cellular_componentGABA-ergic synapse
M1990904cellular_componentribonucleoprotein complex
N0000447biological_processendonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
N0000461biological_processendonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
N0002181biological_processcytoplasmic translation
N0003723molecular_functionRNA binding
N0003735molecular_functionstructural constituent of ribosome
N0005515molecular_functionprotein binding
N0005654cellular_componentnucleoplasm
N0005737cellular_componentcytoplasm
N0005783cellular_componentendoplasmic reticulum
N0005791cellular_componentrough endoplasmic reticulum
N0005829cellular_componentcytosol
N0005840cellular_componentribosome
N0006412biological_processtranslation
N0015935cellular_componentsmall ribosomal subunit
N0022626cellular_componentcytosolic ribosome
N0022627cellular_componentcytosolic small ribosomal subunit
N0045202cellular_componentsynapse
N1990904cellular_componentribonucleoprotein complex
O0002181biological_processcytoplasmic translation
O0003723molecular_functionRNA binding
O0003729molecular_functionmRNA binding
O0003735molecular_functionstructural constituent of ribosome
O0005515molecular_functionprotein binding
O0005634cellular_componentnucleus
O0005654cellular_componentnucleoplasm
O0005730cellular_componentnucleolus
O0005737cellular_componentcytoplasm
O0005829cellular_componentcytosol
O0005840cellular_componentribosome
O0005925cellular_componentfocal adhesion
O0006412biological_processtranslation
O0015935cellular_componentsmall ribosomal subunit
O0016020cellular_componentmembrane
O0017134molecular_functionfibroblast growth factor binding
O0019899molecular_functionenzyme binding
O0022626cellular_componentcytosolic ribosome
O0022627cellular_componentcytosolic small ribosomal subunit
O0045296molecular_functioncadherin binding
O0051443biological_processpositive regulation of ubiquitin-protein transferase activity
O0070062cellular_componentextracellular exosome
O1990904cellular_componentribonucleoprotein complex
P0002181biological_processcytoplasmic translation
P0003723molecular_functionRNA binding
P0003735molecular_functionstructural constituent of ribosome
P0005515molecular_functionprotein binding
P0005634cellular_componentnucleus
P0005654cellular_componentnucleoplasm
P0005730cellular_componentnucleolus
P0005737cellular_componentcytoplasm
P0005783cellular_componentendoplasmic reticulum
P0005829cellular_componentcytosol
P0005840cellular_componentribosome
P0005925cellular_componentfocal adhesion
P0006412biological_processtranslation
P0006413biological_processtranslational initiation
P0022626cellular_componentcytosolic ribosome
P0022627cellular_componentcytosolic small ribosomal subunit
P0030154biological_processcell differentiation
P0032040cellular_componentsmall-subunit processome
P0042274biological_processribosomal small subunit biogenesis
P0043066biological_processnegative regulation of apoptotic process
P0045202cellular_componentsynapse
P0048027molecular_functionmRNA 5'-UTR binding
P0070062cellular_componentextracellular exosome
P1990904cellular_componentribonucleoprotein complex
Q0000028biological_processribosomal small subunit assembly
Q0001618molecular_functionvirus receptor activity
Q0002181biological_processcytoplasmic translation
Q0003677molecular_functionDNA binding
Q0003723molecular_functionRNA binding
Q0003735molecular_functionstructural constituent of ribosome
Q0005055molecular_functionlaminin receptor activity
Q0005515molecular_functionprotein binding
Q0005634cellular_componentnucleus
Q0005654cellular_componentnucleoplasm
Q0005737cellular_componentcytoplasm
Q0005829cellular_componentcytosol
Q0005840cellular_componentribosome
Q0005886cellular_componentplasma membrane
Q0006338biological_processchromatin remodeling
Q0006412biological_processtranslation
Q0007155biological_processcell adhesion
Q0015935cellular_componentsmall ribosomal subunit
Q0016020cellular_componentmembrane
Q0022626cellular_componentcytosolic ribosome
Q0022627cellular_componentcytosolic small ribosomal subunit
Q0043022molecular_functionribosome binding
Q0043236molecular_functionlaminin binding
Q0046718biological_processsymbiont entry into host cell
Q0070062cellular_componentextracellular exosome
Q0140374biological_processantiviral innate immune response
Q1990904cellular_componentribonucleoprotein complex
R0002181biological_processcytoplasmic translation
R0003723molecular_functionRNA binding
R0003729molecular_functionmRNA binding
R0003735molecular_functionstructural constituent of ribosome
R0005515molecular_functionprotein binding
R0005654cellular_componentnucleoplasm
R0005737cellular_componentcytoplasm
R0005783cellular_componentendoplasmic reticulum
R0005791cellular_componentrough endoplasmic reticulum
R0005829cellular_componentcytosol
R0005840cellular_componentribosome
R0006412biological_processtranslation
R0015935cellular_componentsmall ribosomal subunit
R0016020cellular_componentmembrane
R0022626cellular_componentcytosolic ribosome
R0022627cellular_componentcytosolic small ribosomal subunit
R0033119biological_processnegative regulation of RNA splicing
R0045202cellular_componentsynapse
R0045296molecular_functioncadherin binding
R0070062cellular_componentextracellular exosome
R0098556cellular_componentcytoplasmic side of rough endoplasmic reticulum membrane
R1990904cellular_componentribonucleoprotein complex
S0000028biological_processribosomal small subunit assembly
S0002181biological_processcytoplasmic translation
S0003723molecular_functionRNA binding
S0003729molecular_functionmRNA binding
S0003735molecular_functionstructural constituent of ribosome
S0005515molecular_functionprotein binding
S0005634cellular_componentnucleus
S0005654cellular_componentnucleoplasm
S0005730cellular_componentnucleolus
S0005737cellular_componentcytoplasm
S0005783cellular_componentendoplasmic reticulum
S0005829cellular_componentcytosol
S0005840cellular_componentribosome
S0006364biological_processrRNA processing
S0006412biological_processtranslation
S0008284biological_processpositive regulation of cell population proliferation
S0015935cellular_componentsmall ribosomal subunit
S0016020cellular_componentmembrane
S0019901molecular_functionprotein kinase binding
S0022626cellular_componentcytosolic ribosome
S0022627cellular_componentcytosolic small ribosomal subunit
S0030425cellular_componentdendrite
S0031929biological_processTOR signaling
S0032040cellular_componentsmall-subunit processome
S0032868biological_processresponse to insulin
S0036464cellular_componentcytoplasmic ribonucleoprotein granule
S0042274biological_processribosomal small subunit biogenesis
S0042593biological_processglucose homeostasis
S0043065biological_processpositive regulation of apoptotic process
S0044297cellular_componentcell body
S0071361biological_processcellular response to ethanol
S0098793cellular_componentpresynapse
S0098982cellular_componentGABA-ergic synapse
S1903347biological_processnegative regulation of bicellular tight junction assembly
S1990904cellular_componentribonucleoprotein complex
T0000028biological_processribosomal small subunit assembly
T0000122biological_processnegative regulation of transcription by RNA polymerase II
T0002181biological_processcytoplasmic translation
T0003723molecular_functionRNA binding
T0003735molecular_functionstructural constituent of ribosome
T0005515molecular_functionprotein binding
T0005634cellular_componentnucleus
T0005654cellular_componentnucleoplasm
T0005730cellular_componentnucleolus
T0005737cellular_componentcytoplasm
T0005829cellular_componentcytosol
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q0005654cellular_componentnucleoplasm
q0005730cellular_componentnucleolus
q0005737cellular_componentcytoplasm
q0005794cellular_componentGolgi apparatus
q0005829cellular_componentcytosol
q0005840cellular_componentribosome
q0006412biological_processtranslation
q0016020cellular_componentmembrane
q0022626cellular_componentcytosolic ribosome
q0022627cellular_componentcytosolic small ribosomal subunit
q0032040cellular_componentsmall-subunit processome
q0042274biological_processribosomal small subunit biogenesis
q0090263biological_processpositive regulation of canonical Wnt signaling pathway
q1990145biological_processmaintenance of translational fidelity
q1990904cellular_componentribonucleoprotein complex
s0000028biological_processribosomal small subunit assembly
s0002181biological_processcytoplasmic translation
s0003723molecular_functionRNA binding
s0003735molecular_functionstructural constituent of ribosome
s0005515molecular_functionprotein binding
s0005634cellular_componentnucleus
s0005654cellular_componentnucleoplasm
s0005730cellular_componentnucleolus
s0005737cellular_componentcytoplasm
s0005783cellular_componentendoplasmic reticulum
s0005791cellular_componentrough endoplasmic reticulum
s0005829cellular_componentcytosol
s0005840cellular_componentribosome
s0006364biological_processrRNA processing
s0006412biological_processtranslation
s0015935cellular_componentsmall ribosomal subunit
s0022626cellular_componentcytosolic ribosome
s0022627cellular_componentcytosolic small ribosomal subunit
s0030490biological_processmaturation of SSU-rRNA
s0032040cellular_componentsmall-subunit processome
s0042254biological_processribosome biogenesis
s0042274biological_processribosomal small subunit biogenesis
s0045202cellular_componentsynapse
s0070062cellular_componentextracellular exosome
s0098556cellular_componentcytoplasmic side of rough endoplasmic reticulum membrane
s1990904cellular_componentribonucleoprotein complex
v0002181biological_processcytoplasmic translation
v0003723molecular_functionRNA binding
v0003735molecular_functionstructural constituent of ribosome
v0005634cellular_componentnucleus
v0005654cellular_componentnucleoplasm
v0005730cellular_componentnucleolus
v0005737cellular_componentcytoplasm
v0005829cellular_componentcytosol
v0005840cellular_componentribosome
v0005925cellular_componentfocal adhesion
v0006364biological_processrRNA processing
v0006412biological_processtranslation
v0006413biological_processtranslational initiation
v0016020cellular_componentmembrane
v0022626cellular_componentcytosolic ribosome
v0022627cellular_componentcytosolic small ribosomal subunit
v0032040cellular_componentsmall-subunit processome
v0034101biological_processerythrocyte homeostasis
v0042274biological_processribosomal small subunit biogenesis
v1990904cellular_componentribonucleoprotein complex
w0002181biological_processcytoplasmic translation
w0003723molecular_functionRNA binding
w0003735molecular_functionstructural constituent of ribosome
w0005515molecular_functionprotein binding
w0005654cellular_componentnucleoplasm
w0005737cellular_componentcytoplasm
w0005829cellular_componentcytosol
w0005840cellular_componentribosome
w0006412biological_processtranslation
w0015935cellular_componentsmall ribosomal subunit
w0016020cellular_componentmembrane
w0022626cellular_componentcytosolic ribosome
w0022627cellular_componentcytosolic small ribosomal subunit
w0045202cellular_componentsynapse
w0070062cellular_componentextracellular exosome
w0097371molecular_functionMDM2/MDM4 family protein binding
w1901798biological_processpositive regulation of signal transduction by p53 class mediator
w1990904cellular_componentribonucleoprotein complex
w1990948molecular_functionubiquitin ligase inhibitor activity
x0001732biological_processformation of cytoplasmic translation initiation complex
x0002183biological_processcytoplasmic translational initiation
x0002191biological_processcap-dependent translational initiation
x0003723molecular_functionRNA binding
x0003743molecular_functiontranslation initiation factor activity
x0005515molecular_functionprotein binding
x0005737cellular_componentcytoplasm
x0005829cellular_componentcytosol
x0005852cellular_componenteukaryotic translation initiation factor 3 complex
x0006412biological_processtranslation
x0006413biological_processtranslational initiation
x0016020cellular_componentmembrane
x0016282cellular_componenteukaryotic 43S preinitiation complex
x0033290cellular_componenteukaryotic 48S preinitiation complex
x0045202cellular_componentsynapse
x0071541cellular_componenteukaryotic translation initiation factor 3 complex, eIF3m
x0075522biological_processIRES-dependent viral translational initiation
x0075525biological_processviral translational termination-reinitiation
x0098808molecular_functionmRNA cap binding
Functional Information from PROSITE/UniProt
site_idPS00039
Number of Residues9
DetailsDEAD_ATP_HELICASE DEAD-box subfamily ATP-dependent helicases signature. VLDEADEmL
ChainResidueDetails
3VAL180-LEU188

site_idPS00052
Number of Residues27
DetailsRIBOSOMAL_S7 Ribosomal protein S7 signature. ErLtnsMMmhgrnnGKKlmtvrIVkhA
ChainResidueDetails
fGLU70-ALA96

site_idPS00053
Number of Residues18
DetailsRIBOSOMAL_S8 Ribosomal protein S8 signature. GfiVLTTSaGIMdheeAR
ChainResidueDetails
cGLY100-ARG117

site_idPS00054
Number of Residues23
DetailsRIBOSOMAL_S11 Ribosomal protein S11 signature. LrALarS.GMkIgrieDvTPiPSD
ChainResidueDetails
TLEU116-ASP138

site_idPS00055
Number of Residues8
DetailsRIBOSOMAL_S12 Ribosomal protein S12 signature. KqPNSAiR
ChainResidueDetails
aLYS60-ARG67

site_idPS00056
Number of Residues13
DetailsRIBOSOMAL_S17 Ribosomal protein S17 signature. GDiVtVgEcRPLS
ChainResidueDetails
XGLY123-SER135

site_idPS00299
Number of Residues26
DetailsUBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD
ChainResidueDetails
pLYS27-ASP52

site_idPS00323
Number of Residues25
DetailsRIBOSOMAL_S19 Ribosomal protein S19 signature. NGKtfnqveIkpemIGhyLGEFsiT
ChainResidueDetails
jASN98-THR122

site_idPS00360
Number of Residues19
DetailsRIBOSOMAL_S9 Ribosomal protein S9 signature. GGGhvAQiyAirqSiSKAL
ChainResidueDetails
gGLY74-LEU92

site_idPS00361
Number of Residues16
DetailsRIBOSOMAL_S10 Ribosomal protein S10 signature. AkekNLkvkGPVrMPT
ChainResidueDetails
wALA43-THR58

site_idPS00362
Number of Residues31
DetailsRIBOSOMAL_S15 Ribosomal protein S15 signature. VrkHLernRkDkdAkfrLilIesrihrLarY
ChainResidueDetails
VVAL98-TYR128

site_idPS00527
Number of Residues23
DetailsRIBOSOMAL_S14 Ribosomal protein S14 signature. RvCsnrhglirkyg.LNMCRqCFR
ChainResidueDetails
oARG22-ARG44

site_idPS00528
Number of Residues15
DetailsRIBOSOMAL_S4E Ribosomal protein S4e signature. HlKRVAaPkhWmLdK
ChainResidueDetails
YHIS8-LYS22

site_idPS00529
Number of Residues23
DetailsRIBOSOMAL_S24E Ribosomal protein S24e signature. FGggKTtGFGmIYDSldyakknE
ChainResidueDetails
ePHE64-GLU86

site_idPS00548
Number of Residues37
DetailsRIBOSOMAL_S3 Ribosomal protein S3 signature. AKsmkfvdGlMihSgdpVnyyVDtavrhvlLrqGvlG
ChainResidueDetails
hALA147-GLY183

site_idPS00578
Number of Residues12
DetailsRIBOSOMAL_S6E Ribosomal protein S6e signature. ISGGnDkqGfPM
ChainResidueDetails
SILE52-MET63

site_idPS00585
Number of Residues33
DetailsRIBOSOMAL_S5 Ribosomal protein S5 signature. GQrtrFkAfvAIGDyn.GhVGlGvkcsk.EVat.AI
ChainResidueDetails
OGLY119-ILE151

site_idPS00628
Number of Residues20
DetailsRIBOSOMAL_S19E Ribosomal protein S19e signature. PshfsrgSksVaRrVLQaLE
ChainResidueDetails
lPRO89-GLU108

site_idPS00632
Number of Residues25
DetailsRIBOSOMAL_S4 Ribosomal protein S4 signature. LErRLqtqVFKlglAkSihhARvLI
ChainResidueDetails
ZLEU106-ILE130

site_idPS00646
Number of Residues14
DetailsRIBOSOMAL_S13_1 Ribosomal protein S13 signature. RGlRHfwGlrVRGQ
ChainResidueDetails
nARG121-GLN134

site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. ALSGswDgTLRLWDL
ChainResidueDetails
kALA78-LEU92
kILE120-THR134
kILE165-LEU179
kCYS207-LEU221
FVAL67-CYS81

site_idPS00712
Number of Residues16
DetailsRIBOSOMAL_S17E Ribosomal protein S17e signature. IpSKkLRNkIAGYvTH
ChainResidueDetails
vILE41-HIS56

site_idPS00733
Number of Residues8
DetailsRIBOSOMAL_S26E Ribosomal protein S26e signature. YCVSCAIH
ChainResidueDetails
RTYR73-HIS80

site_idPS00948
Number of Residues14
DetailsRIBOSOMAL_S7E Ribosomal protein S7e signature. RLvRELEKKFSgKH
ChainResidueDetails
LARG78-HIS91

site_idPS00961
Number of Residues9
DetailsRIBOSOMAL_S28E Ribosomal protein S28e signature. ESEREARrL
ChainResidueDetails
sGLU60-LEU68

site_idPS00962
Number of Residues12
DetailsRIBOSOMAL_S2_1 Ribosomal protein S2 signature 1. VlKFLAAGTHLG
ChainResidueDetails
QVAL15-GLY26

site_idPS00963
Number of Residues25
DetailsRIBOSOMAL_S2_2 Ribosomal protein S2 signature 2. PrlLVVtDpraDhqpLtEasyvNLP
ChainResidueDetails
QPRO119-PRO143

site_idPS00996
Number of Residues9
DetailsRIBOSOMAL_S21E Ribosomal protein S21e signature. LYVPRKCSA
ChainResidueDetails
NLEU11-ALA19

site_idPS01168
Number of Residues33
DetailsRIBOSOMAL_S27E Ribosomal protein S27e signature. KCpgCykittvFShAqtvvlCvgCStvLcqPtG
ChainResidueDetails
MLYS36-GLY68

site_idPS01189
Number of Residues19
DetailsRIBOSOMAL_S12E Ribosomal protein S12e signature. ALQevLktAlihDGLarGI
ChainResidueDetails
qALA17-ILE35

site_idPS01191
Number of Residues13
DetailsRIBOSOMAL_S3AE Ribosomal protein S3Ae signature. LkGRVfEvSLaDL
ChainResidueDetails
PLEU62-LEU74

site_idPS01193
Number of Residues20
DetailsRIBOSOMAL_S8E Ribosomal protein S8e signature. RrkTGGkrkpy.HkKrKyELG
ChainResidueDetails
dARG11-GLY30

site_idPS01262
Number of Residues23
DetailsIF1A Eukaryotic initiation factor 1A signature. MlGnGRleamCfDGvkRlcHIrG
ChainResidueDetails
GMET41-GLY63

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1063
DetailsDomain: {"description":"PCI","evidences":[{"source":"PROSITE-ProRule","id":"PRU01185","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues124
DetailsRegion: {"description":"Sufficient for interaction with EPAS1","evidences":[{"source":"PubMed","id":"17324924","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues186
DetailsRegion: {"description":"Sufficient for interaction with TRIM27","evidences":[{"source":"PubMed","id":"10504338","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"source":"HAMAP-Rule","id":"MF_03004","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17322308","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Heiserich L.","Gottlieb E.","Matallanas D.","Cooper W.N.","Kolch W."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues264
DetailsDomain: {"description":"MPN","evidences":[{"source":"PROSITE-ProRule","id":"PRU01182","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues33
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"HAMAP-Rule","id":"MF_03005","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17322308","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues21
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues111
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues19
DetailsCompositional bias: {"description":"Low complexity","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"HAMAP-Rule","id":"MF_03007","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17322308","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues38
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues38
DetailsCoiled coil: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03000","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues1
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"source":"HAMAP-Rule","id":"MF_03010","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17322308","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Zebisch A.","Kolch W."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues11
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues30
DetailsRegion: {"description":"Interaction with HSV-1 and HSV-2"}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues71
DetailsDomain: {"description":"S1 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU00180","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI20
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by HRI","evidences":[{"source":"UniProtKB","id":"P83268","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI21
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"38340717","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI22
Number of Residues209
DetailsDomain: {"description":"tr-type G","evidences":[{"source":"PROSITE-ProRule","id":"PRU01059","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI23
Number of Residues7
DetailsRegion: {"description":"G1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01059","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI24
Number of Residues4
DetailsRegion: {"description":"G2","evidences":[{"source":"PROSITE-ProRule","id":"PRU01059","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI25
Number of Residues3
DetailsRegion: {"description":"G3","evidences":[{"source":"PROSITE-ProRule","id":"PRU01059","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI26
Number of Residues3
DetailsRegion: {"description":"G4","evidences":[{"source":"PROSITE-ProRule","id":"PRU01059","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI27
Number of Residues2
DetailsRegion: {"description":"G5","evidences":[{"source":"PROSITE-ProRule","id":"PRU01059","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI28
Number of Residues12
DetailsRegion: {"description":"Interacts with CDC123","evidences":[{"source":"PubMed","id":"35031321","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI29
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P32481","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI30
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9Z0N1","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI31
Number of Residues108
DetailsRepeat: {"description":"WD 1"}
ChainResidueDetails

site_idSWS_FT_FI32
Number of Residues108
DetailsRepeat: {"description":"WD 2"}
ChainResidueDetails

site_idSWS_FT_FI33
Number of Residues129
DetailsRepeat: {"description":"WD 3"}
ChainResidueDetails

site_idSWS_FT_FI34
Number of Residues135
DetailsRepeat: {"description":"WD 4"}
ChainResidueDetails

site_idSWS_FT_FI35
Number of Residues130
DetailsRepeat: {"description":"WD 5"}
ChainResidueDetails

site_idSWS_FT_FI36
Number of Residues119
DetailsRepeat: {"description":"WD 6"}
ChainResidueDetails

site_idSWS_FT_FI37
Number of Residues114
DetailsRepeat: {"description":"WD 7"}
ChainResidueDetails

site_idSWS_FT_FI38
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI39
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)"}
ChainResidueDetails

site_idSWS_FT_FI40
Number of Residues74
DetailsDomain: {"description":"S1-like"}
ChainResidueDetails

site_idSWS_FT_FI41
Number of Residues32
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI42
Number of Residues7
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI43
Number of Residues1
DetailsSite: {"description":"Arginine finger","evidences":[{"source":"PubMed","id":"11166181","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI44
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI45
Number of Residues83
DetailsDomain: {"description":"RRM","evidences":[{"source":"HAMAP-Rule","id":"MF_03001","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI46
Number of Residues42
DetailsRepeat: {"description":"WD 8"}
ChainResidueDetails

site_idSWS_FT_FI47
Number of Residues9
DetailsCompositional bias: {"description":"Polar residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI48
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q8R1B4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI49
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"HAMAP-Rule","id":"MF_03002","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17322308","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI50
Number of Residues6
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI51
Number of Residues13
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI52
Number of Residues46
DetailsZinc finger: {"description":"C4-type","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI53
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"34516797","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7MQ8","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI54
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17081983","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI55
Number of Residues1
DetailsModified residue: {"description":"N-acetylmethionine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2006","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Kanor S.","Tissot J.-D.","Quadroni M."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25944712","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI56
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"25114211","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI57
Number of Residues63
DetailsDomain: {"description":"S5 DRBM","evidences":[{"source":"PROSITE-ProRule","id":"PRU00268","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI58
Number of Residues1
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"28132843","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32011234","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"34469731","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI59
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"PubMed","id":"28132843","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI60
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P97351","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI61
Number of Residues1
DetailsModified residue: {"description":"ADP-ribosyltyrosine","evidences":[{"source":"PubMed","id":"29954836","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI62
Number of Residues59
DetailsRegion: {"description":"Interaction with PPP1R16B","evidences":[{"source":"PubMed","id":"16263087","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI63
Number of Residues19
DetailsRegion: {"description":"Laminin-binding"}
ChainResidueDetails

site_idSWS_FT_FI64
Number of Residues1
DetailsSite: {"description":"Cleavage; by ST3; site 1","evidences":[{"source":"HAMAP-Rule","id":"MF_03016","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI65
Number of Residues1
DetailsSite: {"description":"Cleavage; by ST3; site 2","evidences":[{"source":"HAMAP-Rule","id":"MF_03016","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI66
Number of Residues1
DetailsModified residue: {"description":"N-acetylserine","evidences":[{"source":"HAMAP-Rule","id":"MF_03016","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2004","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Potts A.","Barblan J.","Quadroni M."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25944712","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI67
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P14206","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI68
Number of Residues1
DetailsModified residue: {"description":"ADP-ribosyl glutamic acid","evidences":[{"source":"PubMed","id":"34314702","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI69
Number of Residues1
DetailsModified residue: {"description":"(3R)-3-hydroxyarginine","evidences":[{"source":"PubMed","id":"29563586","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI70
Number of Residues58
DetailsCompositional bias: {"description":"Basic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI71
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI72
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P41035","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI73
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62301","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI74
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P62301","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI75
Number of Residues3
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"36638793","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI76
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P62281","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI77
Number of Residues1
DetailsModified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"UniProtKB","id":"P62281","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI78
Number of Residues1
DetailsLipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"PubMed","id":"21044946","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI79
Number of Residues62
DetailsDomain: {"description":"S4 RNA-binding"}
ChainResidueDetails

site_idSWS_FT_FI80
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P62702","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI81
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q6ZWN5","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI82
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P62267","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI83
Number of Residues1
DetailsModified residue: {"description":"3-hydroxyproline","evidences":[{"source":"PubMed","id":"24550447","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24550462","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28257692","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI84
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P62245","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI85
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P62242","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI86
Number of Residues1
DetailsLipidation: {"description":"N-myristoyl glycine","evidences":[{"source":"PubMed","id":"25255805","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI87
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI88
Number of Residues71
DetailsDomain: {"description":"KH type-2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00118","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI89
Number of Residues1
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Murray L.","Brunton V.G.","Frame M.C.","Calvo F.","Kolch W."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25944712","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI90
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by PKC/PRKCD","evidences":[{"source":"PubMed","id":"19059439","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI91
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by MAPK","evidences":[{"source":"PubMed","id":"15950189","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI92
Number of Residues3
DetailsModified residue: {"description":"Asymmetric dimethylarginine; by PRMT1","evidences":[{"source":"PubMed","id":"19460357","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI93
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by PKB","evidences":[{"source":"PubMed","id":"20605787","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI94
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P62908","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI95
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by IKKB","evidences":[{"source":"PubMed","id":"21399639","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI96
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by CDK1 and PKC/PRKCD","evidences":[{"source":"PubMed","id":"19059439","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21871177","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2009","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Waridel P.","Quadroni M."]}},{"source":"PubMed","id":"16964243","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI97
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"16807684","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI98
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"PubMed","id":"28065601","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28132843","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31981475","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32011234","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"34348161","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"34469731","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI99
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P63325","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI100
Number of Residues1
DetailsModified residue: {"description":"N-acetylthreonine; in Guanine nucleotide-binding protein subunit beta-2-like 1, N-terminally processed","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2006","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Kanor S.","Tissot J.-D.","Quadroni M."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI101
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by ABL1","evidences":[{"source":"PubMed","id":"19423701","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI102
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P68040","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI103
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"11279199","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI104
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by viral VacV B1 kinase","evidences":[{"source":"PubMed","id":"28636603","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI105
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by viral VacV B1 kinase","evidences":[{"source":"PubMed","id":"28636603","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI106
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by viral VacV B1 kinase","evidences":[{"source":"PubMed","id":"28636603","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI107
Number of Residues2
DetailsModified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"PubMed","id":"24129315","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI108
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9CZX8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI109
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9CZX8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI110
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62852","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI111
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25957688","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5A2Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5AJ0","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI112
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25957688","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5A2Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5AJ0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5FLX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5LKS","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI113
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25957688","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5A2Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5AJ0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5LKS","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI114
Number of Residues23
DetailsZinc finger: {"description":"C4-type"}
ChainResidueDetails

site_idSWS_FT_FI115
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P63323","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI116
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P63276","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI117
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI118
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI119
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"36638793","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI120
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P60867","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI121
Number of Residues14
DetailsRegion: {"description":"RNA gate","evidences":[{"source":"UniProtKB","id":"K7IM66","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI122
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"O70194","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI123
Number of Residues342
DetailsDomain: {"description":"Helicase ATP-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI124
Number of Residues161
DetailsDomain: {"description":"Helicase C-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU00542","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI125
Number of Residues56
DetailsMotif: {"description":"Q motif"}
ChainResidueDetails

site_idSWS_FT_FI126
Number of Residues6
DetailsMotif: {"description":"DEAD box"}
ChainResidueDetails

site_idSWS_FT_FI127
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI128
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P60843","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI129
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P60843","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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